The PAW domain (present in PNGases and other worm proteins) is found as a single copy at the C terminus of metazoan peptide:N-glycanase (PNGase) and in multiple copies in hypothetical Caenorhabditis elegans proteins peptide:N-glycanases (PNGases) [(PUBMED:11779830)]. The C-terminal PAW domain of PNGase binds to the mannose moieties of N-linked oligosaccharide chains [(PUBMED:17088551)].

The PAW domain is a slightly elongated molecule and displays a beta-sandwich architecture, which is composed of two layers, containing nine and eight antiparallel beta-strands, respectively, and three additional short helices [(PUBMED:17088551)].

Some proteins known to contain a PAW domain are listed below:

Animal peptide:N-glycanase (PNGase) EC 3.5.1.52, catalyses the deglycosylation of several misfolded N-linked glycoproteins by cleaving the bulky glycan chain before the proteins are degraded by the proteasome.

A systematic computational analysis of protein sequences containing known nuclear domains led to the identification of 28 novel domain families. This represents a 26% increase in the starting set of 107 known nuclear domain families used for the analysis. Most of the novel domains are present in all major eukaryotic lineages, but 3 are species specific. For about 500 of the 1200 proteins that contain these new domains, nuclear localization could be inferred, and for 700, additional features could be predicted. For example, we identified a new domain, likely to have a role downstream of the unfolded protein response; a nematode-specific signalling domain; and a widespread domain, likely to be a noncatalytic homolog of ubiquitin-conjugating enzymes.